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Methods Mol Biol. 2017;1586:11-31. doi: 10.1007/978-1-4939-6887-9_2.

N- and C-Terminal Truncations to Enhance Protein Solubility and Crystallization: Predicting Protein Domain Boundaries with Bioinformatics Tools.

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Department of Biological Sciences, School of Applied Sciences, University of Huddersfield, Queensgate, Huddersfield, West Yorkshire, HD1 3DH, UK.
Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford, Old Road Campus Research Building, Roosevelt Drive, Oxford, Oxfordshire, OX3 7DQ, UK.
Nuffield Department of Orthopaedics, Rheumatology and Musculoskeletal Sciences, Kennedy Institute of Rheumatology, University of Oxford, Old Road Campus, Roosevelt Drive, Oxford, Oxfordshire, OX3 7FY, UK.


Soluble protein expression is a key requirement for biochemical and structural biology approaches to study biological systems in vitro. Production of sufficient quantities may not always be achievable if proteins are poorly soluble which is frequently determined by physico-chemical parameters such as intrinsic disorder. It is well known that discrete protein domains often have a greater likelihood of high-level soluble expression and crystallizability. Determination of such protein domain boundaries can be challenging for novel proteins. Here, we outline the application of bioinformatics tools to facilitate the prediction of potential protein domain boundaries, which can then be used in designing expression construct boundaries for parallelized screening in a range of heterologous expression systems.


Alignment; BLAST; Bioinformatics; Domain; Hidden Markov Model (HMM); PSIPRED; Protein expression; Protein solubility; Protein structure; Secondary structure

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